Enhanced Functionality of Peroxidases by Its Immobilization at the Solid–Liquid Interface of Mesoporous Materials and Nanoparticles

Campos‐Terán, José; Iñarritu, Iker; Aburto, Jorge; Torres, Eduardo

doi:10.1002/9781118523063.ch16

Cited by 3 publications

(2 citation statements)

References 103 publications

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“…This section will summarize the results about the improvement of the laccase biocatalytic behavior applied on the transformation of pharmaceutical compounds, although the main objective was their degradation as micropollutants (Table 3). Current research investigations focused on enzyme immobilization using nanomaterials have shown advantages in terms of the quantity of the immobilized enzyme and the kinetics [99,100]. One remarkable outcome of using nanomaterials is the improvement of the enzyme stability measured as the residual catalytic activity after a given number of reaction cycles.…”

Section: Laccase Immobilizationmentioning

confidence: 99%

Dioxygen Activation by Laccases: Green Chemistry for Fine Chemical Synthesis

2018

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Laccases are enzymes with attractive features for the synthesis of fine chemicals. The friendly reaction conditions of laccases and their high conversion and selectivity make them particularly suitable for green methods of synthesis. In addition, laccases are enzymes with broad substrate variability, ease of production, and no need of cofactors or aggressive oxidizing agents. Among molecules oxidized by laccases are polycyclic aromatic hydrocarbons, azo dyes, pesticides, phenols, and pharmaceuticals. This article reviews the laccase-mediated oxidation of fine chemicals for the production of biologically active compounds. The main aspects of the enzymatic oxidation are summarized; potentials and limitations are identified and proposals to develop more robust catalysts are analyzed.

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Section: Laccase Immobilizationmentioning

confidence: 99%

Dioxygen Activation by Laccases: Green Chemistry for Fine Chemical Synthesis

2018

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“…It is an exceptional protein due to the variety of organic substrates it can accept to perform many different types of oxidation and chlorination reactions [41][42][43][44][45][46][47][48][49][50][51][52][53][54][55][56]. It has been used in previous studies for the degradation of organic molecules and synthesis of organic molecules, and it has been shown to be effective when co-immobilized with GOx [6,51,[57][58][59][60][61][62][63][64][65][66][67][68][69][70][71][72][73][74][75][76]. This study shows that the immobilization of this bienzymatic system via electrostatic interactions is not reusable and activity is almost eliminated after one cycle, presumably due to the leaching of enzymes [62].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of a Bienzymatic System via Crosslinking to a Metal-Organic Framework

et al. 2022

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A leading biotechnological advancement in the field of biocatalysis is the immobilization of enzymes on solid supports to create more stable and recyclable systems. Metal-organic frameworks (MOFs) are porous materials that have been explored as solid supports for enzyme immobilization. Composed of organic linkers and inorganic nodes, MOFs feature empty void space with large surface areas and have the ability to be modified post-synthesis. Our target enzyme system for immobilization is glucose oxidase (GOx) and chloroperoxidase (CPO). Glucose oxidase catalyzes the oxidation of glucose and is used for many applications in biosensing, biofuel cells, and food production. Chloroperoxidase is a fungal heme enzyme that catalyzes peroxide-dependent halogenation, oxidation, and hydroxylation. These two enzymes work sequentially in this enzyme system by GOx producing peroxide, which activates CPO that reacts with a suitable substrate. This study focuses on using a zirconium-based MOF, UiO-66-NH2, to immobilize the enzyme system via crosslinking with the MOF’s amine group on the surface of the MOF. This study investigates two different crosslinkers: disuccinimidyl glutarate (DSG) and 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC)/N-hydroxysuccinidimide (NHS), providing stable crosslinking of the MOF to the enzymes. The two crosslinkers are used to covalently bond CPO and GOx onto UiO-66-NH2, and a comparison of the recyclability and enzymatic activity of the single immobilization of CPO and the doubly immobilized CPO and GOx is discussed through assays and characterization analyses. The DSG-crosslinked composites displayed enhanced activity relative to the free enzyme, and all crosslinked enzyme/MOF composites demonstrated recyclability, with at least 30% of the activity being retained after four catalytic cycles. The results of this report will aid researchers in utilizing CPO as a biocatalyst that is more active and has greater recyclability.

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